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J Biol Chem, Vol. 273, Issue 15, 8849-8859, April 10, 1998
,
From the In Escherichia coli F632, the
14-kilobase pair chromosomal region located between waaC
(formerly rfaC) and waaA (kdtA)
contains genes encoding enzymes required for the synthesis of the type R2 core oligosaccharide portion of lipopolysaccharide. Ten of the 13 open reading frames encode predicted products sharing greater than 90%
total similarity with homologs in E. coli K-12. However, the products of waaK (rfaK) and
waaL (rfaL) each resemble homologs in
Salmonella enterica serovar Typhimurium but
share little similarity with E. coli K-12. The F632 WaaK
and WaaL proteins therefore define differences between the type R2 and
K-12 outer core oligosaccharides of E. coli
lipopolysaccharides. Based on the chemical structure of the core
oligosaccharide of an E. coli F632
waaK::aacC1 mutant and in
vitro glycosyltransferase analyses, waaK encodes
UDP-N-acetylglucosamine:(glucose) lipopolysaccharide
Department of Microbiology, University of
Guelph, Guelph, Ontario, Canada N1G 2W1 and ¶ Institute
for Biological Sciences, National Research Council,
Ottawa, Ontario, Canada K1A OR6
1,2-N-acetylglucosaminyltransferase. The WaaK enzyme
adds a terminal GlcNAc side branch substituent that is crucial for the
recognition of core oligosaccharide acceptor by the O-polysaccharide
ligase, WaaL. Results of complementation analyses of E. coli K-12 and F632 waaL mutants suggest that
structural differences between the WaaL proteins play a role in
recognition of, and interaction with, terminal lipopolysaccharide core
moieties.
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